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• W2107777605 startingPage "461" @default.
• W2107777605 abstract "Recruitment of the 40S ribosome to the 5' end of a eukaryotic mRNA requires assembly of translation initiation factors eIF4E, the cap-binding protein, together with eIF4A and eIF4G into a complex termed eIF4F. While the translational repressor 4E-BP1 regulates binding of eIF4E to eIF4G, the forces required to construct an eIF4F complex remain unidentified. Here, we establish that the herpes simplex virus-1 (HSV-1) ICP6 polypeptide associates with eIF4G to promote eIF4F complex assembly. Strikingly, release of eIF4E from the 4E-BP1 repressor is insufficient to drive complex formation, suggesting that ICP6 is an eIF4F-assembly chaperone. This is the first example of a translation initiation factor-associated protein that promotes active complex assembly and defines a new, controllable step in the initiation of translation. Homology of the N-terminal, eIF4G-binding segment of ICP6 with cellular chaperones suggest that factors capable of interacting with eIF4G and promoting eIF4F complex assembly may play important roles in a variety of processes where translation complexes need to be remodeled or assembled on populations of newly synthesized or derepressed mRNAs, including development, differentiation, and the response to a broad spectrum of environmental cues." @default.
• W2107777605 created "2016-06-24" @default.
• W2107777605 creator A5048434095 @default.
• W2107777605 creator A5055851463 @default.
• W2107777605 date "2006-02-15" @default.
• W2107777605 modified "2023-09-27" @default.
• W2107777605 title "Assembly of an active translation initiation factor complex by a viral protein" @default.
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• W2107777605 doi "https://doi.org/10.1101/gad.1375006" @default.
• W2107777605 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1369048" @default.
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• W2107777605 hasPublicationYear "2006" @default.
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